Skip to main content
PMC home page
Plant Physiology logoLink to Plant Physiology
. 1988 Apr;86(4):987–989. doi: 10.1104/pp.86.4.987

Missense Mutation in the Chlamydomonas Chloroplast Gene that Encodes the Rubisco Large Subunit 1

Robert J Spreitzer 1, Tracy Brown 1,2, Zhixiang Chen 1, Donghong Zhang 1, Souhail R Al-Abed 1
PMCID: PMC1054612  PMID: 16666076

Abstract

The 69-12Q mutant of Chlamydomonas reinhardtii lacks ribulose-1,5-bisphosphate carboxylase activity, but retains holoenzyme protein. It results from a mutation in the chloroplast large-subunit gene that causes an isoleucine-for-threonine substitution at amino-acid residue 173. Considering that lysine-175 is involved in catalysis, it appears that mutations cluster at the active site.

Full text

PDF
987

Images in this article

988Fig. 1
on p.988

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
  2. Church G. M., Gilbert W. Genomic sequencing. Proc Natl Acad Sci U S A. 1984 Apr;81(7):1991–1995. doi: 10.1073/pnas.81.7.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Covarrubias L., Bolivar F. Construction and characterization of new cloning vehicles. VI. Plasmid pBR329, a new derivative of pBR328 lacking the 482-base-pair inverted duplication. Gene. 1982 Jan;17(1):79–89. doi: 10.1016/0378-1119(82)90103-2. [DOI] [PubMed] [Google Scholar]
  4. Dron M., Rahire M., Rochaix J. D., Mets L. First DNA sequence of a chloroplast mutation: a missense alteration in the ribulosebisphosphate carboxylase large subunit gene. Plasmid. 1983 May;9(3):321–324. doi: 10.1016/0147-619x(83)90009-4. [DOI] [PubMed] [Google Scholar]
  5. Dron M., Rahire M., Rochaix J. D. Sequence of the chloroplast DNA region of Chlamydomonas reinhardii containing the gene of the large subunit of ribulose bisphosphate carboxylase and parts of its flanking genes. J Mol Biol. 1982 Dec 25;162(4):775–793. doi: 10.1016/0022-2836(82)90547-2. [DOI] [PubMed] [Google Scholar]
  6. Estelle M., Hanks J., McIntosh L., Somerville C. Site-specific mutagenesis of ribulose-1,5-bisphosphate carboxylase/oxygenase. Evidence that carbamate formation at Lys 191 is required for catalytic activity. J Biol Chem. 1985 Aug 15;260(17):9523–9526. [PubMed] [Google Scholar]
  7. Gutteridge S., Sigal I., Thomas B., Arentzen R., Cordova A., Lorimer G. A site-specific mutation within the active site of ribulose-1,5-bisphosphate carboxylase of Rhodospirillum rubrum. EMBO J. 1984 Dec 1;3(12):2737–2743. doi: 10.1002/j.1460-2075.1984.tb02204.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Miziorko H. M., Lorimer G. H. Ribulose-1,5-bisphosphate carboxylase-oxygenase. Annu Rev Biochem. 1983;52:507–535. doi: 10.1146/annurev.bi.52.070183.002451. [DOI] [PubMed] [Google Scholar]
  9. Niyogi S. K., Foote R. S., Mural R. J., Larimer F. W., Mitra S., Soper T. S., Machanoff R., Hartman F. C. Nonessentiality of histidine 291 of Rhodospirillum rubrum ribulose-bisphosphate carboxylase/oxygenase as determined by site-directed mutagenesis. J Biol Chem. 1986 Aug 5;261(22):10087–10092. [PubMed] [Google Scholar]
  10. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Spreitzer R. J., Goldschmidt-Clermont M., Rahire M., Rochaix J. D. Nonsense mutations in the Chlamydomonas chloroplast gene that codes for the large subunit of ribulosebisphosphate carboxylase/oxygenase. Proc Natl Acad Sci U S A. 1985 Aug;82(16):5460–5464. doi: 10.1073/pnas.82.16.5460. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Spreitzer R. J., Mets L. Photosynthesis-deficient Mutants of Chlamydomonas reinhardii with Associated Light-sensitive Phenotypes. Plant Physiol. 1981 Mar;67(3):565–569. doi: 10.1104/pp.67.3.565. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Stringer C. D., Hartman F. C. Sequences of two active-site peptides from spinach ribulosebisphosphate carboxylase/oxygenase. Biochem Biophys Res Commun. 1978 Feb 28;80(4):1043–1048. doi: 10.1016/0006-291x(78)91351-7. [DOI] [PubMed] [Google Scholar]
  14. Terzaghi B. E., Laing W. A., Christeller J. T., Petersen G. B., Hill D. F. Ribulose 1,5-bisphosphate carboxylase. Effect on the catalytic properties of changing methionine-330 to leucine in the Rhodospirillum rubrum enzyme. Biochem J. 1986 May 1;235(3):839–846. doi: 10.1042/bj2350839. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Wintermans J. F., de Mots A. Spectrophotometric characteristics of chlorophylls a and b and their pheophytins in ethanol. Biochim Biophys Acta. 1965 Nov 29;109(2):448–453. doi: 10.1016/0926-6585(65)90170-6. [DOI] [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES